Taylor S S, Knighton D R, Zheng J, Ten Eyck L F, Sowadski J M
Department of Chemistry, University of California, San Diego, La Jolla 92093-0654.
Faraday Discuss. 1992(93):143-52. doi: 10.1039/fd9929300143.
The structure of the catalytic subunit of cAMP-dependent protein kinase, the first protein kinase structure to be solved, is reviewed. The general architecture of the enzyme is described as well as the active site regions associated with substrate binding and catalysis. In particular, the unique features of the protein kinase nucleotide fold are outlined. While the catalytic subunit is one of the simplest of the protein kinases, it nevertheless serves as a structural framework for the catalytic core of the entire protein kinase family which now includes over 200 important regulatory enzymes. The essential and conserved features of this core are summarized, and a preliminary model of myosin light-chain kinase, based on the structure of the catalytic subunit, is also discussed.
本文综述了环磷酸腺苷（cAMP）依赖性蛋白激酶催化亚基的结构，这是首个被解析的蛋白激酶结构。文中描述了该酶的总体结构，以及与底物结合和催化作用相关的活性位点区域。特别概述了蛋白激酶核苷酸折叠的独特特征。虽然催化亚基是最简单的蛋白激酶之一，但它仍是整个蛋白激酶家族催化核心的结构框架，目前该家族包含200多种重要的调节酶。总结了这一核心的基本和保守特征，并基于催化亚基的结构讨论了肌球蛋白轻链激酶的初步模型。
